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Information on EC 1.15.1.1 - superoxide dismutase and Organism(s) Homo sapiens and UniProt Accession P04179

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EC Tree
IUBMB Comments
A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
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Homo sapiens
UNIPROT: P04179
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
2
+
2
=
+
Synonyms
superoxide dismutase, sod, mnsod, manganese superoxide dismutase, mn-sod, ec-sod, cuznsod, superoxide dismutase 1, cu/zn superoxide dismutase, sod-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
manganese superoxide dismutase
-
copper, zinc superoxide dismutase
-
copper-zinc superoxide dismutase
-
-
-
-
Cu,Zn superoxide dismutase
-
-
Cu,Zn-SOD
-
-
-
-
Cu-Zn superoxide dismutase
-
-
-
-
Cu/Zn superoxide dismutase
-
Cu/Zn superoxide dismutase 1
-
-
cuprein
-
-
-
-
CuZn-SOD
-
-
cytocuprein
-
-
-
-
dismutase, superoxide
-
-
-
-
EC-SOD
ECSOD
-
-
erythrocuprein
-
-
-
-
erythrocyte superoxide dismutase
-
extracellular superoxide dismutase
Fe-SOD
-
-
-
-
ferrisuperoxide dismutase
-
-
-
-
hemocuprein
-
-
-
-
hepatocuprein
-
-
-
-
manganese superoxide dismutase
-
-
Mn-SOD
-
-
-
-
SOD 1
-
-
SOD-1
-
-
-
-
SOD-2
-
-
-
-
SOD-3
-
-
-
-
SOD-4
-
-
-
-
SODF
-
-
-
-
SODS
-
-
-
-
superoxide dismutase
-
-
-
-
superoxide dismutase 1
-
-
superoxide dismutase I
-
-
-
-
superoxide dismutase II
-
-
-
-
superoxide dismutase [Cu-Zn]
UniProt
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 superoxide + 2 H+ = O2 + H2O2
show the reaction diagram
electrostatic guidance of anionic substrate to the active site, detailed overview. Generation of a model for electrostatic-mediated diffusion, and efficient binding of superoxide for catalysis
2 superoxide + 2 H+ = O2 + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
superoxide:superoxide oxidoreductase
A metalloprotein; also known as erythrocuprein, hemocuprein or cytocuprein. Enzymes from most eukaryotes contain both copper and zinc; those from mitochondria and most prokaryotes contain manganese or iron.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-89-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
O2- + H+
O2 + H2O2
show the reaction diagram
O2.- + H+
O2 + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
?
O2.- + H+
O2 + H2O2
show the reaction diagram
-
-
-
?
2 O2.- + 2 H+
O2 + H2O2
show the reaction diagram
-
-
-
-
ir
2 O2.- + 2 H+ +
O2 + H2O2
show the reaction diagram
-
-
-
-
?
2 superoxide + 2 H+
O2 + H2O2
show the reaction diagram
O2.- + H+
O2 + H2O2
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
-
Co2+ binds at zinc site
copper
Cu
-
a Cu,Zn superoxide dismutase
Manganese
-
a MnSOD
Mn
-
a Mn-SOD
Zn
-
a Cu,Zn superoxide dismutase
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
azide
the azide ion acts as a strong competitive inhibitor for SOD by binding directly to the active site metal. Azide is bound end-on at the sixth coordinate position of the manganese ion. Tetrameric electrostatic surfaces are calculated incorporating accurate partial charges for the active site in three states, including a state with superoxide coordinated to the metal using the position of azide as a model
peroxynitrite
almost complete inhibition via nitration of active-site residue Y34, no significant change in conformation upon nitration. Inhibition occurs either through a steric effect of 3-nitrotyrosine 34 that impedes substrate binding or through an electrostatic effect of the nitro group
5,5'-dithiobis(2-nitrobenzoate)
-
Mn-SOD
5-(((2,4-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 630 nM
5-(((3,5-dichlorobenzyl)(ethyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 420 nM
5-(((3,5-dichlorobenzyl)(isopropyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00108 mM
5-(((3,5-dichlorobenzyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 480 nM
5-(((3,5-dichlorobenzyl)(propyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 470 nM
5-(((3,5-dichlorophenethyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00164 mM
5-(((3-(3,5-dichlorophenyl)propyl)(methyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00332 mM
5-((benzyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00245 mM
5-((cyclopropyl(3,5-dichlorobenzyl)amino)methyl)-1H-pyrazol-3(2H)-one
-
EC50 value is 0.00134 mM
5-[(3,5-dichlorophenoxy)methyl]-1,2-dihydro-3H-pyrazol-3-one
-
EC50 value is 400 nM
5-[[(3,5-dichlorophenyl)(methyl)amino]methyl]-1,2-dihydro-3H-pyrazol-3-one
-
EC50 value is 570 nM
CN-
-
extracellular enzyme
di-N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium sulfate
-
EC50 value is 480 nM
diethyldithiocarbamate
iodoacetamide
-
Mn-SOD
Mn(Me-Phimp)2(ClO4)
-
i.e. Mn(2-(1-(2-phenyl-2-(pyridine-2-yl)hydrazono)ethyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2
-
i.e. Mn-(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)naphthalen-1-ol), active as cofactor in superoxide dismutation reaction
Mn(N-Phimp)2(ClO4)
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydrazono)methyl)naphthalen-1-ol)chlorate, active as cofactor in superoxide dismutation reaction
Mn(Phimp)2
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol), active as cofactor in superoxide dismutation reaction
Mn(Phimp)2(ClO4)
-
i.e. Mn(2-((2-phenyl-2-(pyridin-2-yl)hydazono)methyl)phenol)chlorate, active as cofactor in superoxide dismutation reaction
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium chloride
-
EC50 value is 510 nM
-
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium citrate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium dibasic phosphate
-
EC50 value is 480 nM
N-(3,5-dichlorobenzyl)-N-methyl-1-(5-oxo-2,5-dihydro-1H-pyrazol-3-yl)methanaminium L-tartrate
-
EC50 value is 480 nM
O2-
-
substrate inhibition for mutant C140S/Q143A
Penicillamine
-
copper-chelator, wild-type and mutant Cu,Zn-SOD
phenyl mercuric acetate
-
Cu,Zn-SOD
Sodium dodecyl sulfate
-
2% w/v, Cu,Zn-SOD and EC-SOD
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1100 - 40000
O2-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
O2-
-
mutant C140S/Q143A, pH 9.0, 25°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00076
Mn(Me-Phimp)2(ClO4)
Homo sapiens
-
-
0.00112
Mn(N-Phimp)2(ClO4)
Homo sapiens
-
-
0.00029
Mn(Phimp)2
Homo sapiens
-
-
0.00039
Mn(Phimp)2(ClO4)
Homo sapiens
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
assay at
7
-
assay at
7.4
-
assay at
7.4 - 9
assay at
7.8
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.4 - 10.9
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at
22
-
assay at room temperature
25
-
assay at
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
harbors MnSOD with the ala16val polymorphism
Manually annotated by BRENDA team
-
an ovarian carcinoma cell line
Manually annotated by BRENDA team
-
internal mammary arteries
Manually annotated by BRENDA team
-
aortic smooth muscle
Manually annotated by BRENDA team
-
saphenous veins
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MnSOD is translated in the cytoplasm and then imported into the mitochondria via a mitochondrial targeting signal
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
MnSOD ala16val polymorphism is associated with various diseases including breast cancer
malfunction
Role of nitric oxide (NO) modified erythrocytes superoxide dismutase (eSOD) in alopecia areata, a non-scarring hair loss disorder. dysfunctioning of SODis reported in patients with alopecia areata. Protein-A purified IgG of alopecia areata patients (AA-IgG) show strong binding to NO-eSOD in comparison with IgG from controls. In addition, AA-IgG from patients with alopecia universalis recognize NO-eSOD in a greater extentas compared to AA-IgG from patients with patchy persistent alopecia areata. Alopecia universalis patients' sera contain higher levels of NO or carbonyl contents and lower levels of SOD activity compared with patchy persistent alopecia areata patient or control sera
physiological function
superoxide dismutase (SOD) is a prime antioxidant enzymethat destroys the effects of superoxide, thus limiting the dele-terious effects of reactive oxygen and nitrogen species. SOD is considered an important regulator of oxida-tive/nitrosative stress
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SODM_HUMAN
222
0
24750
Swiss-Prot
Mitochondrion (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15800
-
x * 15800, MALDI-TOF-MS
21300
-
4 * 21300, SDS-PAGE
22000
28000
-
4 * 28000, recombinant EC-SOD, SDS-PAGE
32000
35000
-
dimeric wild-type holo-enzyme
38000
-
2 * 38000, recombinant chimera MnSOD-VHb, SDS-PAGE
76000
-
recombinant chimera MnSOD-VHb, gel filtration
88000
additional information
-
primary structure of human erythrocyte enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
dimer
homodimer
-
2 * 38000, recombinant chimera MnSOD-VHb, SDS-PAGE
homotetramer
-
4 * 22000, Mn-SOD, SDS-PAGE
monomer
1 * 33000, recombinant enzyme, SDS-PAGE
monomer or dimer
-
the kinetic mechanism for holo SODs involves native dimer-monomer intermediate, and unfolded monomer, with variable metal dissociation from the monomeric states depending on solution conditions, overview. Naturally occuring mutants seem to favour increased formation of a Zn-free monomer intermediate, which is implicated in the formation of toxic aggregates. Kinetic basis for the extremely high stability of wild-type holo SOD, overview
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of native protein and enzyme nitrated at active site residue Y34, no significant change in conformation upon nitration
mutant enzymes F66A and F66L, hanging drop vapor diffusion method, 0.005 ml of enzyme solution are mixed with 0.005 ml of precipitant solution containing 2.5 M ammonium sulfate, 100 mM imidazole, and 100 mM malic acid, pH 8.5, equilibration against 1 ml of precipitant solution, 1 week, room temperature, X-ray diffraction structure determination and analysis at 2.2 A and 2.3 A resolution, respectively
purified enzyme MnSOD in complex with azide, hanging-drop vapor diffusion, mixing of 0.001 ml of 21 mg/ml protein solution with 0.001 ml of reservoir solution 1.8 M potassium phosphate, pH 7.8, at room temperature for1 day, to obtain the azide complex, 0.002 ml of reservoir containing 200 mM sodium azide are added to drops of 6 day crystals, X-ray diffraction structure determination and analysis at 1.77-1.82 A resolution
crystal structures of unfluorinated and fluorinated enzyme are nearly superimposable. Ratio kcat/Km decreases from 0.8 per mM and s for wild-type to 0.03 per mM and s for the fluorinated mutant which is in significant part due to 3-fluorotyrosine residues distant from the active-site metal
-
enzyme 10 mg per ml in Tris/HCl 50 mM, pH 8.2 by dialysis against ammonium sulfate 2.8 M, pH 8.2, 4°C
-
from recombinant Mn-SOD, asymmetric unit, hanging drop technique, room temperature, equilibration of 3-4 mg/ml enzyme in ammonium phosphate, pH 5.9, plus 10% 2-methyl-2,4-pentanediol against 32% 2-methyl-2,4-pentanediol, X-ray analysis
-
purified recombinant SOD1, hanging drop vapour diffusion, 0.001 ml of 10 mg/ml protein in 50 mM sodium citrate, pH 5.5, 1 mM DTT, 100 mM CuSO4, and 100 mM ZnSO4, is mixed with 0.001 ml of reservoir solution containing 21-25% w/v PEG 4000, 0.1 M sodium acetate, pH 4.2-5.2, X-ray diffraction structure determination and analysis at 3.5 A, molecular replacement
purified zinc-deficient mutant enzyme, 0.002 ml of solution containing 15.7 mg/ml protein in 50 mM Na/K phosphate, pH 7.7, is mixed with 0.002 ml of reservoir solution containing 2.45 M ammonium sulfate, 200 mM NaCl in 50 mM Tris, pH 7.5, room temperature, less than 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution, modelling
recombinant human Cu,Zn-SOD expressed in yeast, hanging drop method by vapour diffusion from 50 mM phosphate, pH 7.7, resulting in 3 different crystal forms
-
wild-type, beta-barrel mutant H43R, dimer interface mutant A4V
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A16V
naturally occuring ala16val polymorphism genotyping, overview
F66A
site-directed mutagenesis, alteration of the active site surrounding, the mutant is 3fold less sensitive to product inhibition compared to the wild-type enzyme
F66L
site-directed mutagenesis, alteration of the active site surrounding, the mutant shows residual product inhibition with formation of a peroxide-inhibited enzyme and increased catalytic activity
A4V
-
mutation causing familial amyotrophic lateral scerosis, 30% of wild-type activity, 1.06 atoms of copper and 1.43 atoms of zinc per subunit
C111S
site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit
C140S
-
catalytic efficiency similar to wild-type, product inhibition is less than in wild-type
C140S/Q143A
-
catalysis does not follow Michaelis-Menten kinetics, substrate inhibition with KI-value of 0.06 mM
D124N
site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit
D124N/C111S
site-directed mutagenesis, the mutant has 0.93 copper and 0.03 zinc per subunit
D83S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
D83S/C111S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
E100G
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
E93A
-
construction of transgenic mice overexpressing wild-type and mutant SOD1, biochemical changes occur in the hindlimb muscle of young, presymptomatic G93A hSOD1 transgenic mice, cdk5 activity is reduced in hindlimb muscle of 27-day-old G93A hSOD1 transgenic mice by suppression through the mutant E93A enzyme, phenotype, overview, mutant G93A SOD1 also suppresses muscle cdk5 activity in vitro
F50E/G51E
-
about 20% of wild-type activity, monomeric
G41N
-
Cu,Zn-SOD, site-directed mutagenesis, analogous to mutant found in familial amyotrophic lateral sclerosis, 47% activity compared to the wild-type
G93R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H46R
-
an amyotrophic lateral sclerosis-associated naturally occuring SOD mutant, misfolding/aggregation mechanism with folding and unfolding kinetics, overview
H63C
-
Cu,Zn-SOD, mutant with exchange of metal-bridging proton-donor His63 for Cys, binds Cu2+, but not Zn2+, 1% remaining activity compared to wild-type
H80S/D83S
site-directed mutagenesis, the mutant has 0.93 copper and 0.08 zinc per subunit
H80S/D83S/C6A/C111S
site-directed mutagenesis, the mutant has 1.07 copper and 1.18 zinc per subunit
N73S
-
ratio kcat/Km about twofold smaller than in wild-type, product inhibition similar to wild-type
N73S/C140S/Q143A
-
catalytic efficiency much smaller than wild-type, no appreciable product inhibition
N73S/Q143A
-
catalytic efficiency much smaller than wild-type, no appreciable product inhibition
Q143A
-
dramatically reduced product inhibition, reduced catalytic activity and efficiency
Y34F
-
about 12fold decrease in kcat value
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
5°C, 1 day, 35% loss of activity
438120
7.2
-
4°C, 1 day, 2% loss of activity
438120
8 - 9.3
-
4°C, 1 day, 10-20% loss of activity
438120
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
wild-type, purified stable for at least 1 week
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
SDS, 1%, complete loss of activity after 6 h
-
urea: 8 M, stable
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
Mn-SOD and Fe-SOD: not stable to organic solvents, Cu,Zn-SOD: stable to organic solvents
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-35°C, protein concentration 45 mg/ml, 50% glycerol
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
soluble recombinant enzyme SOD2 from Escherichia coli cell-free extract by dialysis, anion exchange chromatography, again dialysis, and ultrafiltration
Cu,Zn-SOD
-
Cu,Zn-SOD from erythrocytes
-
Cu,Zn-SOD from liver
-
Cu,Zn-SOD wild-type and mutant recombinant from Escherichia coli
-
Cu,Zn-SOD, wild-type and mutants recombinant from Spodoptera frugiperda cells
-
EC-SOD from aorta
-
EC-SOD recombinant from Escherichia coli as His-tagged protein and partially from insect cells
-
extracellular
-
large scale immunoisolation of native mutant and wildtype SOD1
-
Mn-SOD from liver
-
recombinant chimera MnSOD-VHb from Escherichia coli strain BL21(DE3)
-
recombinant Cu,Zn-SOD
-
recombinant SOD1 from Leishmania tarentolae strain P10 to 90% purity by ultracentrifugation, hydrophobic interaction chromatography and dialysis
recombinant wild-type and truncated mutant FLAG-tagged hEC-SOD enzymes from Spodoptera frugiperda Sf9 cells by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, ala16val polymorphism genotyping, overview, stably expression of human MnSOD-A16 and MnSOD-V16 variants in mouse fibroblasts
gene sod, expression of wild-type and mutant soluble enzymes in Escherichia coli strain QC774, that lacks the genes encoding endogeneous FeSOD, SodB-, and MnSOD, SodA-
gene SOD2, recombinant expression in Escherichia coli
Cu,Zn-SOD, expression of wild-type and mutant in Escherichia coli
-
Cu,Zn-SOD, overexpression in Escherichia coli
-
Cu,Zn-SOD, overexpression of wild-type and mutants in Spodoptera frugiperda cells Sf21 via baculovirus infection
-
EC-SOD, overexpression in Escherichia coli as His-tagged protein and in Tn-5B1-4 cells of Trichoplusia ni via baculovirus infection
-
expression in yeast
-
expression of H63C mutant in Escherichia coli
-
expression of human SOD in Escherichia coli
-
expression of recombinant chimera MnSOD-VHb in Escherichia coli strain BL21(DE3)
-
expression of SOD1 in Leishmania tarentolae strain P10
expression of the CuZn-SOD in Escherichia coli
-
expression of wild-type and mutant enzymes in Escherichia coli
gene sod-1, expression analysis
-
gene SOD3, cloning of EC-SOD and recombinant expression of wild-type and truncated mutant FLAG-tagged hEC-SOD enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method, both full length and truncated hEC-SOD proteins are enzymatically active
Mn-SOD, expression in Escherichia coli
-
overexpression of wild-type and mutant enzymes in hind limb muscle of transgenic mice
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
docosahexaenoic acid inhibits enzyme transcription in cancer cells, involvement of hypoxia-inducible factor-2alpha signaling, but not of peroxisome proliferator-activated receptor alpha, overview. Suppression of SOD-1 expression by clofibrate also requires hypoxia-inducible factor-2alpha and the binding element in the SOD-1 promoter
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
apoprotein expressed in insect cells can be restored by addition of Cu2+, fully active
-
enzyme folding and unfolding kinetic mechanism of wild-type and mutant enzymes at pH 7.8 and 25°C, role of metal ions, overview
-
recombinant EC-SOD refolds from inclusion bodies in E. coli after denaturing
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wagner, U.G.; Werber, M.M.; Beck, Y.; Hartman, J.R.; Frolow, F.; Sussman, J.L.
Characterization of crystals of genetically engineered human manganese superoxide dismutase
J. Mol. Biol.
206
787-788
1989
Homo sapiens, Homo sapiens Mn-SOD
Manually annotated by BRENDA team
Beyer, W.; Imlay, J.; Fridovich, I.
SODs: varieties and distributions. X-ray crystallography of Mn-SODs and Fe-SODs
Prog. Nucleic Acid Res. Mol. Biol.
40
221-253
1991
Synechococcus elongatus PCC 7942 = FACHB-805, Geobacillus stearothermophilus, Bacteroides thetaiotaomicron, Bacteroides fragilis, Saccharomyces cerevisiae, Caulobacter vibrioides, Escherichia coli, Thermus thermophilus, Ginkgo biloba, Halobacterium salinarum, Homo sapiens, Methanobacterium bryantii, Paracoccus denitrificans, Mus musculus, Mycolicibacterium phlei, Nocardia asteroides, Photobacterium leiognathi, Leptolyngbya boryana, Propionibacterium freudenreichii subsp. shermanii, Pseudomonas putida, Rattus norvegicus, Gordonia bronchialis, Streptococcus mutans, Thermoplasma acidophilum, Zea mays, Thermus thermophilus Mn-SOD, Photobacterium leiognathi CuZn-SOD, Caulobacter vibrioides CuZn-SOD, Pseudomonas putida Fe-SOD, Escherichia coli Mn-SOD, Escherichia coli Fe-SOD, Paracoccus denitrificans CuZn-SOD, Geobacillus stearothermophilus Mn-SOD, Thermoplasma acidophilum Fe-SOD
Manually annotated by BRENDA team
Bannister, J.V.; Bannister, W.H.
Isolation and characterization of superoxide dismutase
Methods Enzymol.
105
88-93
1984
Homo sapiens, Photobacterium leiognathi, Pseudomonas putida, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Flohe, L.; tting, F.
Superoxide dismutase assays
Methods Enzymol.
105
93-104
1984
Bos taurus, Homo sapiens, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Matsuda, Y.; Hagashiyama, S.; Kijima, Y.; Suzuki, K.; Kawano, K.; Akiyama, M.; Kawata, S.; Tarui, S.; Deutsch, H.F.; Taniguchi, N.
Human liver manganese superoxide dismutase. Purification and crystallization, subunit association and sulfhydryl reactivity
Eur. J. Biochem.
194
713-720
1990
Homo sapiens, Homo sapiens Mn-SOD
Manually annotated by BRENDA team
Parge, H.E.; Getzoff, E.D.; Scandella, C.S.; Hallewell, R.A.; Tainer, J.A.
Crystallographic characterization of recombinant human CuZn superoxide dismutase
J. Biol. Chem.
261
16215-16218
1986
Homo sapiens, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Jabusch, J.R.; Farb, D.I.; Kerschensteiner, D.A.; Deutsch, H.F.
Some sulfhydryl properties and primary structure of human erythrocyte superoxide dismutase
Biochemistry
19
2310-2316
1980
Homo sapiens, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Briggs, R.G.; Fee, J.A.
Further characterization of human erythrocyte superoxide dismutase
Biochim. Biophys. Acta
537
86-99
1978
Homo sapiens, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Marklund, S.L.
Properties of extracellular superoxide dismutase from human lung
Biochem. J.
220
269-272
1984
Homo sapiens, Homo sapiens Mn-SOD, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Fujii, J.; Myint, T.; Seo, H.G.; Kyanoki, Y.; Ikeda, Y.; Taniguchi, N.
Characterization of wild-type and amyotrophic lateral sclerosis-related mutant Cu,Zn-superoxide dismutases overproduced in baculovirus-infected insect cells
J. Neurochem.
64
1456-1461
1995
Homo sapiens, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Kim, S.M.; Eum, W.S.; Kang, J.H.
Expression, purification, and characterization of a familial amyotrophic lateral sclerosis-associated D90A Cu,Zn-superoxide dismutase mutant
Mol. Cells
8
478-482
1998
Homo sapiens, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Kang, J.H.; Choi, B.J.; Kim, S.M.
Expression and characterization of recombinant human Cu,Zn-superoxide dismutase in Escherichia coli
J. Biochem. Mol. Biol.
30
60-65
1997
Homo sapiens, Homo sapiens CuZn-SOD
-
Manually annotated by BRENDA team
He, H.J.; Yuan, Q.S.; Yang, G.Z.; Wu, X.F.
High-level expression of human extracellular superoxide dismutase in Escherichia coli and insect cells
Protein Expr. Purif.
24
13-17
2002
Homo sapiens
Manually annotated by BRENDA team
Banci, L.; Bertini, I.; Borsari, M.; Viezzoli, M.S.; Hallewell, R.A.
Mutation of the metal-bridging proton-donor His63 residue in human copper, zinc superoxide dismutase. Biochemical and biophysical analysis of the His63-Cys mutant
Eur. J. Biochem.
232
220-225
1995
Homo sapiens, Homo sapiens CuZn-SOD
Manually annotated by BRENDA team
Ahl, I.M.; Lindberg, M.J.; Tibell, L.A.E.
Coexpression of yeast copper chaperone (yCCS) and CuZn-superoxide dismutases in Escherichia coli yields protein with high copper contents
Protein Expr. Purif.
37
311-319
2004
Homo sapiens
Manually annotated by BRENDA team
Agbas, A.; Hui, D.; Wang, X.; Tek, V.; Zaidi, A.; Michaelis, E.K.
Activation of brain calcineurin (Cn) by Cu-Zn superoxide dismutase (SOD1) depends on direct SOD1-Cn protein interactions occurring in vitro and in vivo
Biochem. J.
405
51-59
2007
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Chockalingam, K.; Luba, J.; Nick, H.S.; Silverman, D.N.; Zhao, H.
Engineering and characterization of human manganese superoxide dismutase mutants with high activity and low product inhibition
FEBS J.
273
4853-4861
2006
Homo sapiens
Manually annotated by BRENDA team
Quint, P.; Reutzel, R.; Mikulski, R.; McKenna, R.; Silverman, D.N.
Crystal structure of nitrated human manganese superoxide dismutase: mechanism of inactivation
Free Radic. Biol. Med.
40
453-458
2006
Homo sapiens (P04179), Homo sapiens
Manually annotated by BRENDA team
Kinnula, V.L.; Hodgson, U.A.; Lakari, E.K.; Tan, R.J.; Sormunen, R.T.; Soini, Y.M.; Kakko, S.J.; Laitinen, T.H.; Oury, T.D.; Paeaekkoe, P.K.
Extracellular superoxide dismutase has a highly specific localization in idiopathic pulmonary fibrosis/usual interstitial pneumonia
Histopathology
49
66-74
2006
Homo sapiens
Manually annotated by BRENDA team
Chen, H.L.; Yen, C.C.; Tsai, T.C.; Yu, C.H.; Liou, Y.J.; Lai, Y.W.; Wang, M.L.; Chen, C.M.
Production and characterization of human extracellular superoxide dismutase in the methylotrophic yeast Pichia pastoris
J. Agric. Food Chem.
54
8041-8047
2006
Homo sapiens
Manually annotated by BRENDA team
DiDonato, M.; Craig, L.; Huff, M.E.; Thayer, M.M.; Cardoso, R.M.F.; Kassmann, C.J.; Lo, T.P.; Bruns, C.K.; Powers,E.T.; Kelly, J.W.; Getzoff, E.D; Tainer, J.A.
ALS Mutants o human superoxide dismutase form fibrous aggregates via framework destabilization
J. Mol. Biol.
332
601-615
2003
Homo sapiens
Manually annotated by BRENDA team
Ren, X.; Tu, C.; Bhatt, D.; Perry, J.J.; Tainer, J.A.; Cabelli, D.E.; Silverman, D.N.
Kinetic and structural characterization of human manganese superoxide dismutase containing 3-fluorotyrosines
J. Mol. Struct.
790
168-173
2006
Homo sapiens
-
Manually annotated by BRENDA team
Guzik, T.J.; Olszanecki, R.; Sadowski, J.; Kapelak, B.; Rudzi?ski, P.; Jopek, A.; Kawczynska, A.; Ryszawa, N.; Loster, J.; Jawien, J.; Czesnikiewicz-Guzik, M.; Channon, K.M.; Korbut, R.
Superoxide dismutase activity and expression in human venous and arterial bypass graft vessels
J. Physiol. Pharmacol.
56
313-323
2005
Homo sapiens
Manually annotated by BRENDA team
Zheng, J.; Domsic, J.F.; Cabelli, D.; McKenna, R.; Silverman, D.N.
Structural and kinetic study of differences between human and Escherichia coli manganese superoxide dismutases
Biochemistry
46
14830-14837
2007
Homo sapiens (P04179), Homo sapiens
Manually annotated by BRENDA team
Park, K.H.; Vincent, I.
Presymptomatic biochemical changes in hindlimb muscle of G93A human Cu/Zn superoxide dismutase 1 transgenic mouse model of amyotrophic lateral sclerosis
Biochim. Biophys. Acta
1782
462-468
2008
Homo sapiens
Manually annotated by BRENDA team
Broeyer, F.J.; van Aken, B.E.; Suzuki, J.; Kemme, M.J.; Schoemaker, H.C.; Cohen, A.F.; Mizushima, Y.; Burggraaf, J.
The pharmacokinetics and effects of a long-acting preparation of superoxide dismutase (PC-SOD) in man
Br. J. Clin. Pharmacol.
65
22-29
2008
Homo sapiens
Manually annotated by BRENDA team
Gao, F.; Koenitzer, J.R.; Tobolewski, J.M.; Jiang, D.; Liang, J.; Noble, P.W.; Oury, T.D.
Extracellular superoxide dismutase inhibits inflammation by preventing oxidative fragmentation of hyaluronan
J. Biol. Chem.
283
6058-6066
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Roberts, B.R.; Tainer, J.A.; Getzoff, E.D.; Malencik, D.A.; Anderson, S.R.; Bomben, V.C.; Meyers, K.R.; Karplus, P.A.; Beckman, J.S.
Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS
J. Mol. Biol.
373
877-890
2007
Homo sapiens (P00441), Homo sapiens
Manually annotated by BRENDA team
Suzuki, J.; Broeyer, F.; Cohen, A.; Takebe, M.; Burggraaf, J.; Mizushima, Y.
Pharmacokinetics of PC-SOD, a lecithinized recombinant superoxide dismutase, after single- and multiple-dose administration to healthy Japanese and Caucasian volunteers
J. Clin. Pharmacol.
48
184-192
2008
Homo sapiens
Manually annotated by BRENDA team
Ghosh, K.; Tyagi, N.; Kumar, P.; Singh, U.P.; Goel, N.
Stabilization of Mn(II) and Mn(III) in mononuclear complexes derived from tridentate ligands with N(2)O donors: Synthesis, crystal structure, superoxide dismutase activity and DNA interaction studies
J. Inorg. Biochem.
104
9-18
2009
Homo sapiens
Manually annotated by BRENDA team
Rumfeldt, J.A.; Lepock, J.R.; Meiering, E.M.
Unfolding and folding kinetics of amyotrophic lateral sclerosis-associated mutant Cu,Zn superoxide dismutases
J. Mol. Biol.
385
278-298
2009
Homo sapiens
Manually annotated by BRENDA team
Tuller, E.R.; Beavers, C.T.; Lou, J.R.; Ihnat, M.A.; Benbrook, D.M.; Ding, W.Q.
Docosahexaenoic acid inhibits superoxide dismutase 1 gene transcription in human cancer cells: the involvement of peroxisome proliferator-activated receptor alpha and hypoxia-inducible factor-2alpha signaling
Mol. Pharmacol.
76
588-595
2009
Homo sapiens
Manually annotated by BRENDA team
Gazdag, E.M.; Cirstea, I.C.; Breitling, R.; Lukes, J.; Blankenfeldt, W.; Alexandrov, K.
Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae
Acta Crystallogr. Sect. F
66
871-877
2010
Homo sapiens (P00441), Homo sapiens
Manually annotated by BRENDA team
Isarankura-Na-Ayudhya, C.; Yainoy, S.; Tantimongcolwat, T.; Buelow, L.; Prachayasittikul, V.
Engineering of a novel chimera of superoxide dismutase and Vitreoscilla hemoglobin for rapid detoxification of reactive oxygen species
J. Biosci. Bioeng.
110
633-637
2010
Homo sapiens
Manually annotated by BRENDA team
McAtee, B.; Yager, J.
Manganese superoxide dismutase: Effect of the ala16val polymorphism on protein, activity, and mRNA levels in human breast cancer cell lines and stably transfected mouse embryonic fibroblasts
Mol. Cell. Biochem.
335
107-118
2010
Homo sapiens (P04179), Homo sapiens
Manually annotated by BRENDA team
Rasheed, Z.; Alzolibani, A.A.; Al-Shobaili, H.A.; Saif, G.B.; Al Robaee, A.A.
Biochemical and immunological studies on erythrocytes superoxide dismutase modified by nitric oxide in patients with alopecia areata implications in alopecia patchy persistent and alopecia universalis
Immunol. Lett.
160
50-57
2014
Homo sapiens (P00441), Homo sapiens
Manually annotated by BRENDA team
Zhang, Y.; Zhao, K.T.; Fox, S.G.; Kim, J.; Kirsch, D.R.; Ferrante, R.J.; Morimoto, R.I.; Silverman, R.B.
Tertiary amine pyrazolones and their salts as inhibitors of mutant superoxide dismutase 1-dependent protein aggregation for the treatment of amyotrophic lateral sclerosis
J. Med. Chem.
58
5942-5949
2015
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Azadmanesh, J.; Trickel, S.R.; Borgstahl, G.E.O.
Substrate-analog binding and electrostatic surfaces of human manganese superoxide dismutase
J. Struct. Biol.
199
68-75
2017
Homo sapiens (P04179), Homo sapiens
Manually annotated by BRENDA team
Shrestha, P.; Yun, J.H.; Kim, W.T.; Kim, T.Y.; Lee, W.
Cloning, purification, and characterization of recombinant human extracellular superoxide dismutase in SF9 insect cells
Mol. Cells
39
242-249
2016
Homo sapiens (P08294), Homo sapiens
Manually annotated by BRENDA team